ID V5IHX3_IXORI Unreviewed; 813 AA.
AC V5IHX3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative low-density lipoprotein receptor {ECO:0000313|EMBL:JAB80281.1};
DE Flags: Fragment;
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB80281.1};
RN [1] {ECO:0000313|EMBL:JAB80281.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB80281.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; GANP01004187; JAB80281.1; -; mRNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipoprotein {ECO:0000313|EMBL:JAB80281.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:JAB80281.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 735..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..324
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 412..455
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 456..498
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 499..542
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 543..585
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 4..16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 11..29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 45..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 52..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 85..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 92..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 104..119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 124..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 131..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 143..158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 187..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 206..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 213..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 225..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 255..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB80281.1"
SQ SEQUENCE 813 AA; 90759 MW; C0A0D4032C0F7D23 CRC64;
KRTCSQTEFR CKNGNCIPSR WQCDNENDCE DKSDEDVVTC SNKTCSEEQF TCKSQECIPI
TWRCDGQEDC VDGSDEKDEC LAATCTHEEF SCNNGKCITK RWVCDQDDDC GDGSDEKGCA
NVTCSSAEFM CSNGRCIPDR WHCDGDIDCL DGSDERNCPT TGRPSPCKVR EFQCANGVDC
IHTSWQCDGD PDCPDESDEA NCTNTCRPDQ FQCRNLHCIP GLLECNGKVE CPDRSDEDHC
NTTVNRCNPD SEFDCGGNHC IPKHLVCDGK NDCGAFEDEP RELCHKNECS SGHSGCSDIC
KDDPIGFHCE CHPGFKLTED NRTCDDVDEC LIPGSCSQKC TNYKGGYKCE CIEGYVPEPR
DRHRCKAKEG VPFLLFANRN DIRKINLETG EYVEVVSKLR STIAMDYIYQ TGTVIWSDTV
KEEISSAPID TGAPTKVIIN EDLHVADGLA VDWIYNHVYW TDTAQNLISV ADLDGKNRKA
LFSEDLDEPR AIVVNPLEGW MFWTDWGKQP KIERSGMDGS HRSAIVTTDI LWPNGLAIDF
VSKQLFWVDA KLHLIGSSDY NGNNRRVILS SPILVKHPFS LDVFEDWLYW TDWESEVINK
VNKFTGANLE PVLANGVYSP MDIHVYHSYK TRPQRRRTNC KPANGQCSHL CLPAPSISPH
SAKFSCACPN KMELQEDGHN CRIVETLVST TLRPSTVAAV TDETVVYNAS HNEVSAQPSV
GHEGLAGKAX XXGKLAGIVI GVLGGLAIIF TLIGYVVYRQ CLRRNITSMN FDNPVYRKTT
EDQFSLEKNQ YQPARSYPPS MEPLTSPGTN EFV
//